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RESEARCH PRODUCT

Comparative Studies on IR, Raman, and Surface Enhanced Raman Scattering Spectroscopy of Dipeptides Containing ΔAla and ΔPhe

Jolanta BukowskaMaciej MakowskiAgata KrólikowskaKamilla Malek

subject

Models MolecularSpectrophotometry InfraredSurface PropertiesPhenylalanineAnalytical chemistryMolecular ConformationSpectrum Analysis RamanVibrationMetalchemistry.chemical_compoundsymbols.namesakeAdsorptionDeprotonationSpectrophotometryMaterials ChemistrymedicineCarboxylatePhysical and Theoretical ChemistrySpectroscopyAlaninemedicine.diagnostic_testDipeptidesSurfaces Coatings and FilmsCrystallographychemistryMetalsvisual_artvisual_art.visual_art_mediumsymbolsRaman spectroscopyVisible spectrum

description

Three dipeptides containing dehydroresidues (\DeltaAla, \Delta (Z)Phe, and \Delta (E)Phe) were examined by IR, Raman, and surface-enhanced Raman techniques for the first time. The effect of the size and isomer type of the β -substituent in the dehydroresidue on the conformational structure of the peptide was evaluated by using the analysis of IR and Raman bands. Additionally, SERS spectroscopy provided insight into the adsorption mechanism of these species on the metal surface. SERS spectra were recorded at alkaline pH on the silver sol using visible light excitation. The dehydroresidues studied here strongly influenced the SERS profile of the peptides. The most pronounced SERS signal for all dipeptides was assigned to the symmetric stretching vibration of the carboxylate ions. This indicates that the dehydropeptides studied here primarily adsorb via the deprotonated carboxylic group. Additionally, the enhanced SERS bands in the range 1550 − 1650 cm − 1 show differences in contribution of the dehydroresidue to the adsorption mechanism of the studied peptides.

yearjournalcountryeditionlanguage
2012-01-01Journal of Physical Chemistry B
10.1021/jp208586jhttps://doi.org/10.1021/jp208586j